MolNFT v1 · #65481 · protein

Crystal structure of putative acetyltransferase (YP_001815201.1) from exiguobacterium sp. 255-15 at 1.62 a resolution

3GYA · GCN5-related N-acetyltransferase: “Crystal structure of putative acetyltransferase (YP_001815201.1) from exiguobacterium sp. 255-15 at 1.62 a…”. X-ray diffraction, 2 ligands (COA, SO4), 1 pocket (best druggability 0.58). MolNFT v1…

PDB: 3GYA
Type: protein
Length: 147 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GCN5-related N-acetyltransferase
UniProt: B1YEL6
Ligands: COA, SO4
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GCN5-related N-acetyltransferase	protein	147	32% helix, 26% strand	B1YEL6

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	252	0.58	0.78	28	COA, SO4, EDO

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

3GYA · Crystal structure of putative acetyltransferase (YP_001815201.1) from EXIGUOBACTERIUM SP.… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt B1YEL6
Elsewhere: RCSB PDB 3GYA · PDBe 3GYA · UniProt B1YEL6

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